ALS is a fatal neurodegenerative disease of motor neurons. Toxic aggregates of superoxide dismutase-1 (SOD1) and TAR DNA-binding protein 43 (TDP-43) in motor neurons are characteristic of ALS.The study showed that these two proteins interact such that misfolding of TDP-43 leads to misfolding and aggregation of SOD1 in a cell system and promotes motor neuron damage in zebrafish.
“Publication of these data underscores the connection of misfolded proteins and ALS and supports targeting our TDP-43-specific epitope with PMN267 as a potential therapeutic approach,” stated
The study demonstrated a pathologic synergy between SOD1 and TDP-43 in cell culture and in zebra fish.The interaction between these 2 proteins was characterized at the molecular level.The results indicated that the misfolded TDP-43 epitope previously identified by ProMIS and targeted by PMN267 contains a tryptophan amino acid critical to the pathogenic interaction with SOD1 thereby providing further biological support for the potential of therapeutic intervention with PMN267.
“These findings provide an important contribution to our understanding of ALS/FTLD molecular pathology and continue to validate our approach of targeting misfolded proteins as a therapeutic strategy that translates across multiple neurodegenerative diseases,” said
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